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. 1993 Mar;175(6):1785–1795. doi: 10.1128/jb.175.6.1785-1795.1993

Interaction between the Chlamydia trachomatis histone H1-like protein (Hc1) and DNA.

G Christiansen 1, L B Pedersen 1, J E Koehler 1, A G Lundemose 1, S Birkelund 1
PMCID: PMC203973  PMID: 8449885

Abstract

The gene encoding the Chlamydia trachomatis histone H1-like protein (Hc1) from serovar L2 was cloned into Escherichia coli by use of expression vector pET11d. In this vector, transcription of the gene is under the control of a bacteriophage T7 promoter, and T7 RNA polymerase is inducible in the host. Following induction, the E. coli cells were lysed gently. Gel filtration of the lysate revealed comigration of DNA and Hc1 in the voided volume. Electron microscopy revealed the DNA to be complexed with protein in large aggregates, often in the form of spherical bodies. Purified recombinant Hc1 maintained its DNA-binding capacity and was able at high concentrations to form condensed aggregates with DNA (one molecule of Hc1 per base pair) independently of the form or size of the DNA but with a slight preference for supercoiled DNA. Hc1 alone is thus able to package DNA into condensed spherical bodies.

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